UniProtKB - Q6B856 (TBB2B_BOVIN)
Protein
Tubulin beta-2B chain
Gene
TUBB2B
Organism
Bos taurus (Bovine)
Status
Functioni
Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. Plays a critical role in proper axon guidance in both central and peripheral axon tracts. Implicated in neuronal migration.By similarity
GO - Molecular functioni
- GTPase activity Source: InterPro
- GTP binding Source: GO_Central
- protein heterodimerization activity Source: UniProtKB
- structural constituent of cytoskeleton Source: GO_Central
GO - Biological processi
- microtubule-based process Source: UniProtKB
- microtubule cytoskeleton organization Source: GO_Central
- mitotic cell cycle Source: GO_Central
- positive regulation of axon guidance Source: UniProtKB
Keywordsi
Biological process | Neurogenesis |
Ligand | GTP-binding, Nucleotide-binding |
Enzyme and pathway databases
Reactomei | R-BTA-190840, Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane R-BTA-2467813, Separation of Sister Chromatids R-BTA-2500257, Resolution of Sister Chromatid Cohesion R-BTA-3371497, HSP90 chaperone cycle for steroid hormone receptors (SHR) R-BTA-380320, Recruitment of NuMA to mitotic centrosomes R-BTA-5610787, Hedgehog 'off' state R-BTA-5617833, Cilium Assembly R-BTA-5620924, Intraflagellar transport R-BTA-5626467, RHO GTPases activate IQGAPs R-BTA-5663220, RHO GTPases Activate Formins R-BTA-6807878, COPI-mediated anterograde transport R-BTA-6811434, COPI-dependent Golgi-to-ER retrograde traffic R-BTA-68877, Mitotic Prometaphase R-BTA-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint R-BTA-8955332, Carboxyterminal post-translational modifications of tubulin R-BTA-9646399, Aggrephagy R-BTA-9648025, EML4 and NUDC in mitotic spindle formation R-BTA-9668328, Sealing of the nuclear envelope (NE) by ESCRT-III R-BTA-983189, Kinesins |
Names & Taxonomyi
Protein namesi | Recommended name: Tubulin beta-2B chain |
Gene namesi | Name:TUBB2B |
Organismi | Bos taurus (Bovine) |
Taxonomic identifieri | 9913 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Proteomesi |
|
Subcellular locationi
Cytoskeleton
- cytoskeleton By similarity
Cytoskeleton
- microtubule Source: GO_Central
- microtubule cytoskeleton Source: UniProtKB
Other locations
- cytoplasm Source: GO_Central
Keywords - Cellular componenti
Cytoplasm, Cytoskeleton, MicrotubulePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000262654 | 1 – 445 | Tubulin beta-2B chainAdd BLAST | 445 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 40 | PhosphoserineBy similarity | 1 | |
Modified residuei | 55 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 58 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 58 | N6-succinyllysine; alternateBy similarity | 1 | |
Cross-linki | 58 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity | ||
Modified residuei | 172 | Phosphoserine; by CDK1By similarity | 1 | |
Modified residuei | 285 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 290 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 318 | Omega-N-methylarginineBy similarity | 1 | |
Cross-linki | 324 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Modified residuei | 438 | 5-glutamyl polyglutamateBy similarity | 1 |
Post-translational modificationi
Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear.By similarity
Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (By similarity). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity).By similarity
Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules.By similarity
Keywords - PTMi
Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
PaxDbi | Q6B856 |
PeptideAtlasi | Q6B856 |
PRIDEi | Q6B856 |
PTM databases
iPTMneti | Q6B856 |
Expressioni
Gene expression databases
Bgeei | ENSBTAG00000004093, Expressed in prefrontal cortex and 17 other tissues |
Interactioni
Subunit structurei
Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.
By similarityGO - Molecular functioni
- protein heterodimerization activity Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 158875, 3 interactors |
DIPi | DIP-47524N |
IntActi | Q6B856, 7 interactors |
MINTi | Q6B856 |
STRINGi | 9913.ENSBTAP00000005346 |
Chemistry databases
BindingDBi | Q6B856 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SASBDBi | Q6B856 |
SMRi | Q6B856 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q6B856 |
Family & Domainsi
Sequence similaritiesi
Belongs to the tubulin family.Curated
Phylogenomic databases
eggNOGi | KOG1375, Eukaryota |
InParanoidi | Q6B856 |
OMAi | ESCEYLQ |
OrthoDBi | 962471at2759 |
TreeFami | TF300298 |
Family and domain databases
Gene3Di | 1.10.287.600, 1 hit 3.30.1330.20, 1 hit 3.40.50.1440, 1 hit |
InterProi | View protein in InterPro IPR013838, Beta-tubulin_BS IPR002453, Beta_tubulin IPR008280, Tub_FtsZ_C IPR000217, Tubulin IPR018316, Tubulin/FtsZ_2-layer-sand-dom IPR037103, Tubulin/FtsZ_C_sf IPR036525, Tubulin/FtsZ_GTPase_sf IPR023123, Tubulin_C IPR017975, Tubulin_CS IPR003008, Tubulin_FtsZ_GTPase |
PANTHERi | PTHR11588, PTHR11588, 1 hit |
Pfami | View protein in Pfam PF00091, Tubulin, 1 hit PF03953, Tubulin_C, 1 hit |
PRINTSi | PR01163, BETATUBULIN PR01161, TUBULIN |
SMARTi | View protein in SMART SM00864, Tubulin, 1 hit SM00865, Tubulin_C, 1 hit |
SUPFAMi | SSF52490, SSF52490, 1 hit SSF55307, SSF55307, 1 hit |
PROSITEi | View protein in PROSITE PS00227, TUBULIN, 1 hit PS00228, TUBULIN_B_AUTOREG, 1 hit |
i Sequence
Sequence statusi: Complete.
Q6B856-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY
60 70 80 90 100
YNEATGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN
110 120 130 140 150
WAKGHYTEGA ELVDSVLDVV RKESESCDCL QGFQLTHSLG GGTGSGMGTL
160 170 180 190 200
LISKIREEYP DRIMNTFSVM PSPKVSDTVV EPYNATLSVH QLVENTDETY
210 220 230 240 250
CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDSKNMM
310 320 330 340 350
AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK
360 370 380 390 400
TAVCDIPPRG LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG
410 420 430 440
EGMDEMEFTE AESNMNDLVS EYQQYQDATA DEQGEFEEEE GEDEA
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 201 | C → S in AAT84374 (Ref. 1) Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY675081 mRNA Translation: AAT84374.1 |
RefSeqi | NP_001003900.1, NM_001003900.1 |
Genome annotation databases
GeneIDi | 281555 |
KEGGi | bta:281555 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY675081 mRNA Translation: AAT84374.1 |
RefSeqi | NP_001003900.1, NM_001003900.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1SA0 | X-ray | 3.58 | B/D | 1-439 | [»] | |
1SA1 | X-ray | 4.20 | B/D | 1-439 | [»] | |
1TVK | X-ray | 2.89 | B | 1-427 | [»] | |
1Z2B | X-ray | 4.10 | B/D | 1-445 | [»] | |
2P4N | electron microscopy | 9.00 | B | 1-445 | [»] | |
2WBE | electron microscopy | 9.40 | B | 1-445 | [»] | |
2XRP | electron microscopy | 8.20 | A/C/E/G | 1-445 | [»] | |
3DCO | electron microscopy | 1.90 | B | 1-445 | [»] | |
3DU7 | X-ray | 4.10 | B/D | 1-445 | [»] | |
3E22 | X-ray | 3.80 | B/D | 1-445 | [»] | |
3IZ0 | electron microscopy | 8.60 | B | 1-445 | [»] | |
3J1T | electron microscopy | 9.70 | C | 1-427 | [»] | |
3J1U | electron microscopy | 9.70 | C | 1-427 | [»] | |
3J2U | electron microscopy | 10.80 | B/D | 1-445 | [»] | |
4AQV | electron microscopy | 9.70 | B | 1-445 | [»] | |
4AQW | electron microscopy | 9.50 | B | 1-445 | [»] | |
4ATU | electron microscopy | 8.30 | A/C/E/G | 1-445 | [»] | |
4ATX | electron microscopy | 8.20 | A | 1-445 | [»] | |
4CK5 | electron microscopy | 10.00 | B | 1-445 | [»] | |
4CK6 | electron microscopy | 9.20 | B | 1-445 | [»] | |
4CK7 | electron microscopy | 9.20 | B | 1-445 | [»] | |
4I4T | X-ray | 1.80 | B/D | 1-445 | [»] | |
4I50 | X-ray | 2.30 | B/D | 1-445 | [»] | |
4I55 | X-ray | 2.20 | B/D | 1-445 | [»] | |
4IHJ | X-ray | 2.00 | B/D | 1-445 | [»] | |
4IIJ | X-ray | 2.60 | B/D | 1-445 | [»] | |
4O2A | X-ray | 2.50 | B/D | 1-445 | [»] | |
4O2B | X-ray | 2.30 | B/D | 1-445 | [»] | |
4O4H | X-ray | 2.10 | B/D | 1-445 | [»] | |
4O4I | X-ray | 2.40 | B/D | 1-445 | [»] | |
4O4J | X-ray | 2.20 | B/D | 1-445 | [»] | |
4O4L | X-ray | 2.20 | B/D | 1-445 | [»] | |
4TUY | X-ray | 2.10 | B/D | 1-445 | [»] | |
4TV8 | X-ray | 2.10 | B/D | 1-445 | [»] | |
4TV9 | X-ray | 2.00 | B/D | 1-445 | [»] | |
4UXO | electron microscopy | 6.30 | B | 1-445 | [»] | |
4UXP | electron microscopy | 6.30 | B | 1-445 | [»] | |
4UXR | electron microscopy | 7.00 | B | 1-445 | [»] | |
4UXS | electron microscopy | 7.00 | B | 1-445 | [»] | |
4UXT | electron microscopy | 7.40 | B | 1-445 | [»] | |
4UXY | electron microscopy | 6.50 | B | 1-445 | [»] | |
4UY0 | electron microscopy | 7.70 | B | 2-427 | [»] | |
4YJ2 | X-ray | 2.60 | B/D | 1-445 | [»] | |
4YJ3 | X-ray | 3.75 | B/D | 1-445 | [»] | |
5EIB | X-ray | 2.10 | D | 1-445 | [»] | |
5EZY | X-ray | 2.05 | B/D | 1-445 | [»] | |
5GON | X-ray | 2.48 | B/D | 1-431 | [»] | |
5H74 | X-ray | 2.60 | B/D | 1-445 | [»] | |
5H7O | X-ray | 2.80 | B/D | 1-445 | [»] | |
5HNW | electron microscopy | 6.60 | B | 2-445 | [»] | |
5HNX | electron microscopy | 6.60 | B | 1-445 | [»] | |
5HNY | electron microscopy | 6.30 | B | 2-427 | [»] | |
5HNZ | electron microscopy | 5.80 | B | 1-445 | [»] | |
5ITZ | X-ray | 2.20 | B | 1-445 | [»] | |
5IYZ | X-ray | 1.80 | B/D | 1-445 | [»] | |
5J2T | X-ray | 2.20 | B/D | 1-445 | [»] | |
5J2U | X-ray | 2.50 | B/D | 1-445 | [»] | |
5JH7 | X-ray | 2.25 | B/D | 1-445 | [»] | |
5JVD | X-ray | 2.39 | B/D | 1-445 | [»] | |
5LA6 | X-ray | 2.10 | B/D | 1-445 | [»] | |
5LOV | X-ray | 2.40 | B/D | 1-445 | [»] | |
5LP6 | X-ray | 2.90 | B/D | 1-445 | [»] | |
5LXS | X-ray | 2.20 | B/D | 1-445 | [»] | |
5LXT | X-ray | 1.90 | B/D | 1-445 | [»] | |
5LYJ | X-ray | 2.40 | B/D | 1-445 | [»] | |
5M50 | electron microscopy | 5.30 | B/E | 1-427 | [»] | |
5M54 | electron microscopy | 8.00 | B/E | 2-427 | [»] | |
5M5C | electron microscopy | 4.80 | B/E | 2-427 | [»] | |
5M5I | electron microscopy | 9.30 | B | 1-445 | [»] | |
5M5L | electron microscopy | 9.30 | B | 1-445 | [»] | |
5M5M | electron microscopy | 9.30 | B | 1-445 | [»] | |
5M5N | electron microscopy | 9.30 | B | 1-445 | [»] | |
5M5O | electron microscopy | 9.30 | B | 1-445 | [»] | |
5M7E | X-ray | 2.05 | B/D | 1-445 | [»] | |
5M7G | X-ray | 2.25 | B/D | 1-445 | [»] | |
5M8D | X-ray | 2.25 | B/D | 1-445 | [»] | |
5M8G | X-ray | 2.15 | B/D | 1-445 | [»] | |
5MF4 | X-ray | 2.30 | B/D | 1-445 | [»] | |
5ND2 | electron microscopy | 5.80 | B | 1-445 | [»] | |
5ND3 | electron microscopy | 6.10 | B | 1-445 | [»] | |
5ND4 | electron microscopy | 4.40 | B | 2-427 | [»] | |
5ND7 | electron microscopy | 7.90 | B | 1-445 | [»] | |
5NFZ | X-ray | 2.10 | B/D | 1-445 | [»] | |
5NG1 | X-ray | 2.20 | B/D | 1-445 | [»] | |
5NJH | X-ray | 2.39 | B/D | 1-445 | [»] | |
5NM5 | X-ray | 2.05 | B | 1-445 | [»] | |
5NQT | X-ray | 2.15 | B | 1-445 | [»] | |
5NQU | X-ray | 1.80 | B | 1-445 | [»] | |
5O7A | X-ray | 2.50 | B/D | 1-445 | [»] | |
5OSK | X-ray | 2.11 | B/D | 1-445 | [»] | |
5OV7 | X-ray | 2.40 | B/D | 1-445 | [»] | |
5XAF | X-ray | 2.55 | B/D | 1-445 | [»] | |
5XAG | X-ray | 2.56 | B/D | 1-445 | [»] | |
5XLT | X-ray | 2.81 | B/D | 1-445 | [»] | |
5XLZ | X-ray | 2.30 | B/D | 1-445 | [»] | |
5YZ3 | X-ray | 2.54 | B/D | 1-445 | [»] | |
5Z4P | X-ray | 2.50 | B | 1-428 | [»] | |
D | 1-431 | [»] | ||||
5Z4U | X-ray | 3.18 | B/D | 1-445 | [»] | |
5ZXH | X-ray | 2.80 | B/D | 1-445 | [»] | |
6AGK | X-ray | 2.80 | B/D | 1-445 | [»] | |
6BBN | X-ray | 3.51 | B/D | 1-445 | [»] | |
6EG5 | X-ray | 2.45 | B/D | 1-445 | [»] | |
6F7C | X-ray | 2.00 | B/D | 1-445 | [»] | |
6FII | X-ray | 2.40 | B/D | 1-445 | [»] | |
6FJF | X-ray | 2.40 | B/D | 1-445 | [»] | |
6FJM | X-ray | 2.10 | B/D | 1-445 | [»] | |
6FKJ | X-ray | 2.15 | B/D | 1-445 | [»] | |
6FKL | X-ray | 2.10 | B/D | 1-445 | [»] | |
6GF3 | X-ray | 2.40 | B/D | 1-445 | [»] | |
6GJ4 | X-ray | 2.40 | B/D | 1-445 | [»] | |
6GZE | X-ray | 2.49 | B/D | 1-445 | [»] | |
6HX8 | X-ray | 2.40 | B/D | 1-445 | [»] | |
6I5C | X-ray | 2.95 | B/D | 1-445 | [»] | |
6JCJ | X-ray | 2.50 | B/D | 1-445 | [»] | |
6K9V | X-ray | 2.54 | B/D | 1-445 | [»] | |
6KNZ | X-ray | 2.48 | B/D | 1-445 | [»] | |
6N47 | X-ray | 2.60 | B/D | 1-445 | [»] | |
6OJQ | electron microscopy | 3.67 | B | 1-426 | [»] | |
6QQN | X-ray | 2.30 | B/D | 1-445 | [»] | |
6QTN | X-ray | 1.90 | B/D | 1-445 | [»] | |
6REV | electron microscopy | 3.80 | B/b | 1-429 | [»] | |
6RF2 | electron microscopy | 4.20 | B/b | 1-429 | [»] | |
6RF8 | electron microscopy | 3.80 | B/b | 1-429 | [»] | |
6RFD | electron microscopy | 3.90 | B/b | 1-429 | [»] | |
6S8K | X-ray | 1.52 | B | 1-445 | [»] | |
6S9E | X-ray | 2.25 | B/D | 1-445 | [»] | |
6SES | X-ray | 2.00 | B/D | 1-445 | [»] | |
6WVL | electron microscopy | 3.20 | B/D | 1-445 | [»] | |
6WVM | electron microscopy | 3.30 | B/D | 1-445 | [»] | |
6WVR | electron microscopy | 2.90 | B/D | 1-445 | [»] | |
6Y6D | X-ray | 2.20 | B/D | 1-445 | [»] | |
SASBDBi | Q6B856 | |||||
SMRi | Q6B856 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 158875, 3 interactors |
DIPi | DIP-47524N |
IntActi | Q6B856, 7 interactors |
MINTi | Q6B856 |
STRINGi | 9913.ENSBTAP00000005346 |
Chemistry databases
BindingDBi | Q6B856 |
ChEMBLi | CHEMBL3394 |
DrugCentrali | Q6B856 |
PTM databases
iPTMneti | Q6B856 |
Proteomic databases
PaxDbi | Q6B856 |
PeptideAtlasi | Q6B856 |
PRIDEi | Q6B856 |
Genome annotation databases
GeneIDi | 281555 |
KEGGi | bta:281555 |
Organism-specific databases
CTDi | 347733 |
Phylogenomic databases
eggNOGi | KOG1375, Eukaryota |
InParanoidi | Q6B856 |
OMAi | ESCEYLQ |
OrthoDBi | 962471at2759 |
TreeFami | TF300298 |
Enzyme and pathway databases
Reactomei | R-BTA-190840, Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane R-BTA-2467813, Separation of Sister Chromatids R-BTA-2500257, Resolution of Sister Chromatid Cohesion R-BTA-3371497, HSP90 chaperone cycle for steroid hormone receptors (SHR) R-BTA-380320, Recruitment of NuMA to mitotic centrosomes R-BTA-5610787, Hedgehog 'off' state R-BTA-5617833, Cilium Assembly R-BTA-5620924, Intraflagellar transport R-BTA-5626467, RHO GTPases activate IQGAPs R-BTA-5663220, RHO GTPases Activate Formins R-BTA-6807878, COPI-mediated anterograde transport R-BTA-6811434, COPI-dependent Golgi-to-ER retrograde traffic R-BTA-68877, Mitotic Prometaphase R-BTA-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint R-BTA-8955332, Carboxyterminal post-translational modifications of tubulin R-BTA-9646399, Aggrephagy R-BTA-9648025, EML4 and NUDC in mitotic spindle formation R-BTA-9668328, Sealing of the nuclear envelope (NE) by ESCRT-III R-BTA-983189, Kinesins |
Miscellaneous databases
EvolutionaryTracei | Q6B856 |
PROi | PR:Q6B856 |
Gene expression databases
Bgeei | ENSBTAG00000004093, Expressed in prefrontal cortex and 17 other tissues |
Family and domain databases
Gene3Di | 1.10.287.600, 1 hit 3.30.1330.20, 1 hit 3.40.50.1440, 1 hit |
InterProi | View protein in InterPro IPR013838, Beta-tubulin_BS IPR002453, Beta_tubulin IPR008280, Tub_FtsZ_C IPR000217, Tubulin IPR018316, Tubulin/FtsZ_2-layer-sand-dom IPR037103, Tubulin/FtsZ_C_sf IPR036525, Tubulin/FtsZ_GTPase_sf IPR023123, Tubulin_C IPR017975, Tubulin_CS IPR003008, Tubulin_FtsZ_GTPase |
PANTHERi | PTHR11588, PTHR11588, 1 hit |
Pfami | View protein in Pfam PF00091, Tubulin, 1 hit PF03953, Tubulin_C, 1 hit |
PRINTSi | PR01163, BETATUBULIN PR01161, TUBULIN |
SMARTi | View protein in SMART SM00864, Tubulin, 1 hit SM00865, Tubulin_C, 1 hit |
SUPFAMi | SSF52490, SSF52490, 1 hit SSF55307, SSF55307, 1 hit |
PROSITEi | View protein in PROSITE PS00227, TUBULIN, 1 hit PS00228, TUBULIN_B_AUTOREG, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | TBB2B_BOVIN | |
Accessioni | Q6B856Primary (citable) accession number: Q6B856 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 28, 2006 |
Last sequence update: | November 28, 2006 | |
Last modified: | December 2, 2020 | |
This is version 148 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families